ArticleProteins2008
The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway.
Article in Proteins, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 29 citations in OpenAlex.
- Structural analysis of YcdY, a member of the redox-enzyme maturation protein family.Acta crystallographica. Section F, Structural biology communications · 2025Article
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization.Protein expression and purification · 2017Article
- Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD.Microbiology (Reading, England) · 2016Article
- NarJ subfamily system specific chaperone diversity and evolution is directed by respiratory enzyme associations.BMC evolutionary biology · 2015Article
- Biosynthesis and Insertion of the Molybdenum Cofactor.EcoSal Plus · 2015Review
- Unique Photobleaching Phenomena of the Twin-Arginine Translocase Respiratory Enzyme Chaperone DmsD.The open biochemistry journal · 2014Article
- Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway.The Biochemical journal · 2013Article
- Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone.PloS one · 2012Article
- Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Structural analysis of a monomeric form of the twin-arginine leader peptide binding chaperone Escherichia coli DmsD.Journal of molecular biology · 2009Article
- The twin-arginine signal peptide of Bacillus subtilis YwbN can direct either Tat- or Sec-dependent secretion of different cargo proteins: secretion of active subtilisin via the B. subtilis Tat pathway.Applied and environmental microbiology · 2008Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The DmsD protein is necessary for the biogenesis of dimethyl sulphoxide (DMSO) reductase in many prokaryotes. It performs a critical chaperone function initiated through its binding to the twin-arginine signal peptide of DmsA, the catalytic subunit of DMSO reductase. Upon binding to DmsD, DmsA is translocated to the periplasm via the so-called twin-arginine translocation (Tat) pathway. Here we report the 1.38 A crystal structure of the protein DmsD from Salmonella typhimurium and compare it with a close functional homolog, TorD. DmsD has an all-alpha fold structure with a notable helical extension located at its N-terminus with two solvent exposed hydrophobic residues. A major difference between DmsD and TorD is that TorD structure is a domain-swapped dimer, while DmsD exists as a monomer. Nevertheless, these two proteins have a number of common features suggesting they function by using similar mechanisms. A possible signal peptide-binding site is proposed based on structural similarities. Computational analysis was used to identify a potential GTP binding pocket on similar surfaces of DmsD and TorD structures.
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